RAD23B Antikörper

Produktnummer ABIN6241895

Produktdetails anti-RAD23B Antikörper

Target: RAD23B (RAD23 Homolog B (RAD23B))

Reaktivität: Human, Maus

Wirt: Maus

Klonalität: Monoklonal

Konjugat: Dieser RAD23B Antikörper ist unkonjugiert

Applikation: Western Blotting (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC)

Immunogen: Recombinant Protein

Anwendungsinformationen

Applikationshinweise: WB: 1:1000. IHC: 1:100. ICC: 1:100

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Lagerung: 4 °C,-20 °C

Details zu RAD23B

Target: RAD23B (RAD23 Homolog B (RAD23B))

Andere Bezeichnung: hHR23b (RAD23B Produkte)

Synonyme: HHR23B antikoerper, HR23B antikoerper, P58 antikoerper, 0610007D13Rik antikoerper, AV001138 antikoerper, mHR23B antikoerper, p58 antikoerper, MGC107846 antikoerper, zgc:65951 antikoerper, RAD23 homolog B, nucleotide excision repair protein antikoerper, UV excision repair protein RAD23 homolog B antikoerper, RAD23 homolog B, nucleotide excision repair protein S homeolog antikoerper, RAD23B antikoerper, Rad23b antikoerper, rd23b antikoerper, rad23b antikoerper, rad23b.S antikoerper

Hintergrund: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum- associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER, it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.

UniProt: P54727

Pathways: DNA Reparatur